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Use of Synthetic Peptides in the Dissection of Protein-Targeting Interactions

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Protein Targeting Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 88))

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Abstract

Phosphorylation of protein substrates by kinases and phosphatases is a major process in the control of cellular function (1). The mechanisms involved in the regulation of kinase and phosphatase activity have been the subject of intense investigation since glycogen phosphorylase was first recognized to be regulated by phosphorylation (2,3). The use of synthetic peptides has featured extensively in structure and function studies, establishing regions that are important for the control of substrate phosphorylation. The regulation of kinases and phosphatases is achieved at many levels. One level of regulation involves the subcellular localization of kinases and phosphatases through interactions with targeting proteins. This chapter will focus on the use of synthetic peptides in the identification of functional domains on targeting proteins, the characterization of bioactive peptides in vitro, and the use of peptides to disrupt enzyme localization in cells.

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Authors and Affiliations

  1. Vollum Institute, Oregon Health Sciences University, Portland, OR

    John D. Scott & Maree C. Faux

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  1. John D. Scott
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  2. Maree C. Faux
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Editors and Affiliations

  1. Hannah Research Institute, Scotland, UK

    Roger A. Clegg

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© 1998 Humana Press Inc.

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Scott, J.D., Faux, M.C. (1998). Use of Synthetic Peptides in the Dissection of Protein-Targeting Interactions. In: Clegg, R.A. (eds) Protein Targeting Protocols. Methods in Molecular Biology™, vol 88. Humana Press. https://doi.org/10.1385/0-89603-487-9:161

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  • DOI: https://doi.org/10.1385/0-89603-487-9:161

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-487-7

  • Online ISBN: 978-1-59259-572-3

  • eBook Packages: Springer Protocols

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